PSAA_GLOVI
ID PSAA_GLOVI Reviewed; 783 AA.
AC Q7NFT6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1;
DE EC=1.97.1.12;
DE AltName: Full=PsaA;
GN Name=psaA; OrderedLocusNames=glr3438;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CHARACTERIZATION OF PHOTOSYSTEM I.
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=15589832; DOI=10.1016/j.febslet.2004.11.013;
RA Inoue H., Tsuchiya T., Satoh S., Miyashita H., Kaneko T., Tabata S.,
RA Tanaka A., Mimuro M.;
RT "Unique constitution of photosystem I with a novel subunit in the
RT cyanobacterium Gloeobacter violaceus PCC 7421.";
RL FEBS Lett. 578:275-279(2004).
CC -!- FUNCTION: PsaA and PsaB bind P700, the primary electron donor of
CC photosystem I (PSI), as well as the electron acceptors A0, A1 and FX.
CC PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase,
CC converting photonic excitation into a charge separation, which
CC transfers an electron from the donor P700 chlorophyll pair to the
CC spectroscopically characterized acceptors A0, A1, FX, FA and FB in
CC turn. Oxidized P700 is reduced on the lumenal side of the thylakoid
CC membrane by plastocyanin or cytochrome c6.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin]
CC = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:29036,
CC ChEBI:CHEBI:30212, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:49552; EC=1.97.1.12;
CC -!- COFACTOR:
CC Note=PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2
CC phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll
CC a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a
CC chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1
CC is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur
CC center. {ECO:0000250};
CC -!- SUBUNIT: The PsaA/B heterodimer binds the P700 chlorophyll special pair
CC and subsequent electron acceptors. PSI consists of a core antenna
CC complex that captures photons, and an electron transfer chain that
CC converts photonic excitation into a charge separation. The G.violaceus
CC PSI reaction center is composed of one copy each of PsaA,B,C,D,E,F,L,M
CC and Z, and forms trimeric complexes.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000045; BAC91379.1; -; Genomic_DNA.
DR RefSeq; NP_926384.1; NC_005125.1.
DR RefSeq; WP_011143427.1; NC_005125.1.
DR PDB; 7F4V; EM; 2.04 A; aA/bA/cA=1-783.
DR PDBsum; 7F4V; -.
DR AlphaFoldDB; Q7NFT6; -.
DR SMR; Q7NFT6; -.
DR STRING; 251221.35214010; -.
DR EnsemblBacteria; BAC91379; BAC91379; BAC91379.
DR KEGG; gvi:glr3438; -.
DR PATRIC; fig|251221.4.peg.3470; -.
DR eggNOG; COG2885; Bacteria.
DR HOGENOM; CLU_016126_1_0_3; -.
DR InParanoid; Q7NFT6; -.
DR OMA; TWAFFHA; -.
DR OrthoDB; 32023at2; -.
DR PhylomeDB; Q7NFT6; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.1130.10; -; 1.
DR HAMAP; MF_00458; PSI_PsaA; 1.
DR InterPro; IPR006243; PSI_PsaA.
DR InterPro; IPR001280; PSI_PsaA/B.
DR InterPro; IPR020586; PSI_PsaA/B_CS.
DR InterPro; IPR036408; PSI_PsaA/B_sf.
DR PANTHER; PTHR30128:SF61; PTHR30128:SF61; 1.
DR Pfam; PF00223; PsaA_PsaB; 1.
DR PIRSF; PIRSF002905; PSI_A; 1.
DR PRINTS; PR00257; PHOTSYSPSAAB.
DR SUPFAM; SSF81558; SSF81558; 1.
DR TIGRFAMs; TIGR01335; psaA; 1.
DR PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cell inner membrane; Cell membrane; Chlorophyll;
KW Chromophore; Electron transport; Iron; Iron-sulfur; Magnesium; Membrane;
KW Metal-binding; Oxidoreductase; Photosynthesis; Photosystem I;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..783
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088585"
FT TRANSMEM 72..95
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..185
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..225
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..316
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..376
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..418
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..462
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..568
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..629
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..719
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255"
FT TRANSMEM 757..777
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255"
FT BINDING 592
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 601
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 708
FT /ligand="chlorophyll a'"
FT /ligand_id="ChEBI:CHEBI:189419"
FT /ligand_label="A1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 716
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 724
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000250"
FT BINDING 725
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
SQ SEQUENCE 783 AA; 86419 MW; A6200C1B9755CCEE CRC64;
MSTTPQEREK PVRVLVDNDP VPTSTEKWGK PGWFERNLAR GPKTTTWIWD LHALAHDFET
HTSDKEEISR KIFSAHFGHL AVVCVWLSGM FWHGAYFSNF TAWMENPLGL KPSAQTVWPV
FGQEILNDPS TVAKGFEQGG IVITSGLFHL WRAVGFTTTG QLAAMSIAML IIAALFLFAG
WFHYHKRAPK LEWFQNVESM LNHHLAGLFG LGSLFWTGHL IHVALPVKAQ LDAGIAPAQV
NPFAGLDYGL MGQYFPKGFG PNGGLGAFFT LNWGQFTDFL TFKGGLEPAT GALYLTDIAH
HHLAIATLFI IAGHMYRTNW GIGHSIKEML EAHKGPLTGE GHRGLYEVLT TSWHAQLAIN
LAMAGSITII VAHHMYAMNP YPYMGTDYAT QISLFTHHMW IGGFLIVGAG AHAAIFMVRD
YDPVTNQNNL LDRVLRHRDA IISHLNWVTL FLGFHSFGLY VHNDTMQALG RPRDMFADFA
IPLQPVFAQW IQNIHAAAPG GATAPWVGGT SPTWYTGALS SAATLQANQV LALANDKISI
SPIHLGTADF MVHHIFALCI HVTVLILLKG VLFARSSRLI PDKANLGFRF PCDGPGRGGT
CQSSAWDHVF LGLFWMYNTI SVVIFHFSWK MQSDVWGTVD RSTGAVNHII GNTDVLLGGQ
TVALSQYAAS SININGWLRD FLWAQSSAVI NSYGGPLSAY GLMFLGAHFI WAFSLMFLFS
GRGYWQELIE SIVWAHNKLK VAPAIQPRAL SITQGRAVGV AHYLLGGIAT TWAFFLARFL
ALP
